Recent Advances on Synaptotagmin-Like Mitochondrial-Lipid Binding Protein Domain Containing Lipid Transfer Proteins.

Contact (Thousand Oaks (Ventura County, Calif.)) Pub Date : 2024-08-13 eCollection Date: 2024-01-01 DOI:10.1177/25152564241273646
Xuewen Hu, Yirui Cai, Wei-Ke Ji
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引用次数: 0

Abstract

The Synaptotagmin-like mitochondrial-lipid binding protein (SMP) domain is found in a group of ER-resident lipid transfer proteins that are recruited to membrane contact sites (MCSs) by adaptors. Deciphering the molecular basis underlying the recruitment of SMP proteins to specific MCS sheds light not only on their cellular localization but also on their biological functions at these sites. Here we summarize recent advances in SMP domain-containing lipid transfer proteins, focusing on a recent study showing the localization, regulation and cellular function of a specific SMP protein named testis expressed protein 2 (Tex2). TMEM55, a potential PIP phosphatase on late endosome/lysosomal (LE/lys) membranes, was identified as an adaptor that enables the recruitment of Tex2 to ER- LE/lys MCS. In addition, we have summarized several important questions about the regulation and physiological functions of Tex2 that remained unanswered.

Abstract Image

Abstract Image

突触表蛋白-类线粒体-脂质结合蛋白结构域含脂质转移蛋白的最新研究进展。
线粒体脂质结合蛋白(SMP)结构域是一组常驻ER的脂质转移蛋白,它们被适配体招募到膜接触位点(MCS)。破译 SMP 蛋白被招募到特定 MCS 的分子基础不仅能揭示它们的细胞定位,还能揭示它们在这些位点的生物功能。在此,我们总结了含 SMP 结构域的脂质转移蛋白的最新研究进展,重点介绍一种名为睾丸表达蛋白 2(Tex2)的特异性 SMP 蛋白的定位、调控和细胞功能。TMEM55是晚期内膜体/溶酶体(LE/lys)膜上一种潜在的PIP磷酸酶,它被鉴定为一种适配体,能使Tex2被招募到ER- LE/lys MCS上。此外,我们还总结了有关 Tex2 的调控和生理功能的几个重要问题,这些问题仍未得到解答。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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CiteScore
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